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Q9NRE1 (MMP26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-26

Short name=MMP-26
EC=3.4.24.-
Alternative name(s):
Endometase
Matrilysin-2
Gene names
Name:MMP26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Expressed specifically in uterus and placenta. Is also widely expressed in malignant tumors from different sources as well as in diverse tumor cell lines.

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similarities

Belongs to the peptidase M10A family.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMGlycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Non-traceable author statement Ref.2. Source: UniProtKB

   Cellular_componentproteinaceous extracellular matrix

Non-traceable author statement Ref.3. Source: UniProtKB

   Molecular_functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 8972 By similarity
PRO_0000028855
Chain90 – 261172Matrix metalloproteinase-26
PRO_0000028856

Regions

Motif80 – 878Cysteine switch By similarity

Sites

Active site2091 By similarity
Metal binding821Zinc; in inhibited form By similarity
Metal binding2081Zinc; catalytic By similarity
Metal binding2121Zinc; catalytic By similarity
Metal binding2181Zinc; catalytic By similarity

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation2211N-linked (GlcNAc...) Potential

Natural variations

Natural variant431K → E. Ref.3 Ref.4
Corresponds to variant rs2499953 [ dbSNP | Ensembl ].
VAR_033489
Natural variant2601I → M.
Corresponds to variant rs16908114 [ dbSNP | Ensembl ].
VAR_033490

Experimental info

Sequence conflict711M → I in AAF80180. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NRE1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: A66D0DBE3ED7DE76

FASTA26129,708
        10         20         30         40         50         60 
MQLVILRVTI FLPWCFAVPV PPAADHKGWD FVEGYFHQFF LTKKESPLLT QETQTQLLQQ 

        70         80         90        100        110        120 
FHRNGTDLLD MQMHALLHQP HCGVPDGSDT SISPGRCKWN KHTLTYRIIN YPHDMKPSAV 

       130        140        150        160        170        180 
KDSIYNAVSI WSNVTPLIFQ QVQNGDADIK VSFWQWAHED GWPFDGPGGI LGHAFLPNSG 

       190        200        210        220        230        240 
NPGVVHFDKN EHWSASDTGY NLFLVATHEI GHSLGLQHSG NQSSIMYPTY WYHDPRTFQL 

       250        260 
SADDIQRIQH LYGEKCSSDI P 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of MMP-26 A novel matrilysin-like proteinase."
Begnoit de Coignac A., Elson G.C.A., Delneste Y., Magistrelli G., Jeannin P., Aubry J.-P., Berthier O., Schmitt D., Bonnefoy J.-Y., Gauchat J.-F.
Eur. J. Biochem. 267:3323-3329(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity."
Uria J.A., Lopez-Otin C.
Cancer Res. 60:4745-4751(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Identification and characterization of Homo sapiens endometase (matrix metalloproteinase-26) from endometrial tumor."
Park H.I., Ni J., Gerkema F.E., Liu D., Belozerov V.E., Sang Q.-X.A.
J. Biol. Chem. 275:20540-20544(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-43.
[4]"Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin."
Marchenko G.N., Ratnikov B.I., Rozanov D.V., Godzik A., Deryugina E.I., Strongin A.Y.
Biochem. J. 356:705-718(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-43.
Tissue: Kidney.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF230354 mRNA. Translation: AAF80180.1.
AJ251531 mRNA. Translation: CAC08821.1.
AF248646 mRNA. Translation: AAF82359.1.
AF291664 mRNA. Translation: AAG00603.1.
AF291665 Genomic DNA. Translation: AAG02470.1.
BC101541 mRNA. Translation: AAI01542.1.
BC101543 mRNA. Translation: AAI01544.1.
CCDSCCDS7752.1.
RefSeqNP_068573.2. NM_021801.3.
UniGeneHs.204732.

3D structure databases

ProteinModelPortalQ9NRE1.
SMRQ9NRE1. Positions 31-253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000300762.

Chemistry

BindingDBQ9NRE1.
ChEMBLCHEMBL4707.

Protein family/group databases

MEROPSM10.029.

PTM databases

PhosphoSiteQ9NRE1.

Polymorphism databases

DMDM13629493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300762; ENSP00000300762; ENSG00000167346.
ENST00000380390; ENSP00000369753; ENSG00000167346.
GeneID56547.
KEGGhsa:56547.
UCSCuc001lzv.3. human.

Organism-specific databases

CTD56547.
GeneCardsGC11P004726.
HGNCHGNC:14249. MMP26.
HPAHPA022022.
MIM605470. gene.
neXtProtNX_Q9NRE1.
PharmGKBPA30883.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236071.
HOGENOMHOG000239471.
HOVERGENHBG052484.
InParanoidQ9NRE1.
KOK08004.
OMAVTPLIFQ.
OrthoDBEOG7K3TMK.
PhylomeDBQ9NRE1.
TreeFamTF315428.

Gene expression databases

BgeeQ9NRE1.
CleanExHS_MMP26.
GenevestigatorQ9NRE1.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR028736. MMP26.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PANTHERPTHR10201:SF76. PTHR10201:SF76. 1 hit.
PfamPF00413. Peptidase_M10. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP26.
GenomeRNAi56547.
NextBio62031.
PMAP-CutDBQ9NRE1.
PROQ9NRE1.
SOURCESearch...

Entry information

Entry nameMMP26_HUMAN
AccessionPrimary (citable) accession number: Q9NRE1
Secondary accession number(s): Q3MJ78, Q9GZS2, Q9NR87
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM